The bioremediation of hydrocarbon in contaminated soils by mixed cultures of hydrocarbondegrading bacteria was investigated. The mixtures or consortia of bacteria, denoted as Consortium 1 and Consortium 2 consisted of 3 and 6 bacterial strains, respectively. Bacterial strains used in this study were from the Center for Research in Enzymes and Microbiology (CREAM) collection of strains, at Universiti Putra Malaysia, and were isolated from hydrocarbon-contaminated soil samples by enrichments on either crude oil or individual hydrocarbons as the sole carbon source. The strains were selected based on the criteria that they were able to display good growth in crude oil, individual hydrocarbon compounds or both. Their ability to degrade hydrocarbon contamination in the environment was investigated using soil samples that were contaminated with diesel, crude oil or engine oil. Consortium 2, which consisted of 6 bacterial strains, was more efficient at removing the medium-and long-chain alkanes in the diesel-contaminated soil compared to Consortium 1. Further, Consortium 2 could effectively remove the medium-and long-chain alkanes in the engine oil such that the alkanes were undetectable after a 30-day incubation period. Consortium 2 consisted predominantly of Bacillus and Pseudomonas spp.

An organic solvent-tolerant S5 lipase was purified by affinity chromatography and anion exchange chromatography. The molecular mass of the lipase was estimated to be 60 kDa with 387 purification fold. The optimal temperature and pH were 45 degrees C and 9.0, respectively. The purified lipase was stable at 45 degrees C and pH 6-9. It exhibited the highest stability in the presence of various organic solvents such as n-dodecane, 1-pentanol, and toluene. Ca2+ and Mg2+ stimulated lipase activity, whereas EDTA had no effect on its activity. The S5 lipase exhibited the highest activity in the presence of palm oil as a natural oil and triolein as a synthetic triglyceride. It showed random positional specificity on the thin-layer chromatography.

The synthesis of wax ester using refined, bleached and deodorized (RBD) palm oil and oleyl alcohol catalyzed by lipozyme IM was carried out. Response surface methodology (RSM) based on a five-level, four-variable central composite rotatable design (CCRD) was used to evaluate the interactive effects of synthesis, of reaction time (2.5-10 h), temperature (30-70 °C), amount of enzyme (0.1-0.2 g) and substrate molar ratio (palm oil to oleyl alcohol, 1:1-1:5) on the percentage yield of wax esters. The optimum conditions derived via RSM were: reaction time 7.38 h, temperature 53.9 °C, amount of enzyme 0.149 g, and substrate molar ratio 1:3.41. The actual experimental yield was 84.6% under optimum condition, which compared well to the maximum predicted value of 85.4%.

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Background: Thermostable bacterial lipases occupy a place of prominence among biocatalysts owing to their novel, multifold applications and resistance to high temperature and other operational conditions. The capability of lipases to catalyze a variety of novel reactions in both aqueous and nonaqueous media presents a fascinating field for research, creating interest to isolate novel lipase producers and optimize lipase production. The most important stages in a biological process are modeling and optimization to improve a system and increase the efficiency of the process without increasing the cost.

The physical factors affecting the production of an organic solvent-tolerant protease from Pseudomonas aeruginosa strain K was investigated. Growth and protease production were detected from 37 to 45 degrees C with 37 degrees C being the optimum temperature for P. aeruginosa. Maximum enzyme activity was achieved at static conditions with 4.0% (v/v) inoculum. Shifting the culture from stationary to shaking condition decreased the protease production (6.0-10.0% v/v). Extracellular organic solvent-tolerant protease was detected over a broad pH range from 6.0 to 9.0. However, the highest yield of protease was observed at pH 7.0. Neutral media increased the protease production compared to acidic or alkaline media.

Background: Many researchers have reported on the optimization of protease production; nevertheless, only a few have reported on the optimization of the production of organic solventtolerant proteases. Ironically, none has reported on thermostable organic solvent-tolerant protease to date. The aim of this study was to isolate the thermostable organic solvent-tolerant protease and identify the culture conditions which support its production. The bacteria of genus Bacillus are active producers of extra-cellular proteases, and the thermostability of enzyme production by Bacillus species has been well-studied by a number of researchers. In the present study, the Bacillus subtilis strain Rand was isolated from the contaminated soil found in Port Dickson, Malaysia.